Abstract
Abalone (Haliotis discus hannai) is an important commercial seafood species. Pleopod muscle is the edible part of abalone, which is rich in protein and mainly composed of myofibril protein and collagen. This study used the method of grading extraction solution, scanning electronic microscopy (SEM), and Fourier transform infrared (FTIR) to investigate the law of changes in chemical interactions and textural properties of the abalone (Haliotis discus hannai Ino) pleopod muscle protein. The results indicate that as the temperature increases, the changes of chemical interaction in the center and the edge or transition part of the abalone muscle protein were similar. Our results not only expose the change of the secondary structure of the abalone muscle protein during the heating-gel forming process but also provide information on the relationship between chemical interactions and textural properties. The study provides useful information on the mechanism of protein changes in the pleopod muscle of abalone during heating and on the processing techniques of the abalone muscle.